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anti-Human ATP6V0D2 Antibodies:
anti-Mouse (Murine) ATP6V0D2 Antibodies:
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Arabidopsis thaliana Polyclonal ATP6V0D2 Primary Antibody for IHC, WB - ABIN3197488
Hinton, Sennoune, Bond, Fang, Reuveni, Sahagian, Jay, Martinez-Zaguilan, Forgac: Function of a subunit isoforms of the V-ATPase in pH homeostasis and in vitro invasion of MDA-MB231 human breast cancer cells. in The Journal of biological chemistry 2009
Show all 10 Pubmed References
Human Monoclonal ATP6V0D2 Primary Antibody for ELISA, WB - ABIN566966
Teramachi, Zhou, Subler, Kitagawa, Galson, Dempster, Windle, Kurihara, Roodman: Increased IL-6 expression in osteoclasts is necessary but not sufficient for the development of Paget's disease of bone. in Journal of bone and mineral research : the official journal of the American Society for Bone and Mineral Research 2014
Show all 2 Pubmed References
Cow (Bovine) Polyclonal ATP6V0D2 Primary Antibody for WB - ABIN2786234
Morel: Neurotransmitter release: the dark side of the vacuolar-H+ATPase. in Biology of the cell / under the auspices of the European Cell Biology Organization 2003
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Human Polyclonal ATP6V0D2 Primary Antibody for IF (p), IHC (p) - ABIN1714597
Jayachandran, Lugo, Heiling, Miller, Rule, Lieske: Extracellular vesicles in urine of women with but not without kidney stones manifest patterns similar to men: a case control study. in Biology of sex differences 2015
gammadelta T cells suppressed iDCs osteoclastogenesis by downregulation of the RANK/cFos/ATP6V0D2 signaling pathway.
The secondary structures of d1 and d2 subunits were highly similar, but the relative stability against thermal stress was higher for d1 than d2.
these data suggest that Adrm1, a new Atp6v0d2-interacting protein, plays an important role in osteoclast differentiation, and in particular the fusion of preosteoclasts.
High V-ATPase expression is associated with Bone Pain Induced by Multiple Myeloma.
we propose that PTH has a direct effect on osteoblasts and osteoclasts, and that this effect is mediated through PTH1R, thus contributing to bone remodeling
Insulin significantly activated ERK1/2 MAP kinase as well as markedly induced the expression of NFATc1, an osteoclast marker gene, and Atp6v0d2, an osteoclast fusion-related gene.
V-ATPase has a role in modulating a macrophage phenotype towards tumor-associated macrophages through the action of the a2 isoform of V-ATPase
Luteolin can be effective in reducing bone resorption and that this effect of luteolin may be through disruption of osteoclast V-ATPase a3-d2 interaction.
PKCdelta deficiency does not perturb formation of the ruffled border or trafficking of lysosomal vesicles containing the vacuolar-ATPase (v-ATPase).
these findings suggest that the critical role of ATP6v0d2 may be limited to the control of bone homeostasis under normal development.
The data indicate that integrity of lipid rafts regulates the activity of V-ATPase in osteoclasts, suggesting that cholesterol-lowering agents might be useful for inhibiting osteoclast-dependent bone resorption.
d2 is expressed mainly in kidney and at lower levels in heart, spleen, skeletal muscle, and testis. The d2 isoform can complement the yeast vma6Delta phenotype when cells are grown at 25, but not 30, degrees C.
d2 mRNA and protein appear later during nephrogenesis than does the ubiquitously expressed E1 subunit
d2 protein displayed association with membranes and the localization in lysosomes and antigen-containing endosomes.
Atp6v0d2 is a regulator of osteoclast fusion and bone formation.
Data indicate for the first time that the NFATc1/Atp6v0d2 and DC-STAMP signaling axis plays a key role in the osteoclast multinucleation process, which is essential for efficient bone resorption.
Atp6v0d2 (d2), an isoform of the d subunit in the V-ATPase, showed 5-fold higher expression than that of Atp6v0d1 (d1) in mature osteoclasts, indicating a potential function in osteoclastic bone resorption.
MEF2 and MITF function cooperatively with NFATc1 to transactivate the V-ATPase d2 promoter during RANKL-induced osteoclastogenesis.
Subunit of the integral membrane V0 complex of vacuolar ATPase. Vacuolar ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells, thus providing most of the energy required for transport processes in the vacuolar system (By similarity). May play a role in coupling of proton transport and ATP hydrolysis. Regulator of osteoclast fusion and bone formation.
V-ATPase subunit d 2
, V-type proton ATPase subunit d 2
, vacuolar proton pump subunit d 2
, ATPase, H+ transporting, V0 subunit D
, osteoclast-specific vacuolar ATP synthase
, vacuolar proton-translocating ATPase d subunit d2
, ATPase, H+ transporting, lysosomal 38kDa, V0 subunit d2
, ATPase, H+ transporting, lysosomal 38kDa, V0 subunit d
, Vacuolar proton pump subunit d 2
, ATPase, H+ transporting, lysosomal V0 subunit D2